Author

Tom Scheidt

Johannes Gutenberg University MainzORCID 0000-0002-0185-7730Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

Click to filter author papers

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 2 Organism:human· 2 Assay:protein structure· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

Alexander J. DeariD· 1 shared Anđela ŠarićiD· 1 shared Carla SchmidtiD· 1 shared Dev ThackeriD· 1 shared Dorothee DormanniD· 1 shared Edward A. LemkeiD· 1 shared Elin StemmeiD· 1 shared Emil AxelliD· 1 shared

Activity by Year

2026-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

1 shared paperBiophysics

Alexander J. DearORCID

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

A Phosphorylation-Induced Micellization switch in the low complexity domain of TDP-43

Rodrigo F. Dillenburg, Lopatina Anastasia, Hao Ruan, Tom Scheidt, Simone Mosna, Emre Pekbilir, Julia Hesselbarth, Frank Schafer-Depoix, Katharina Landfester, Carla Schmidt, Martin M. Möckel, Svenja Morsbach, Friederike Schmid, Dorothee Dormann, Lukas S. Stelzl, , Edward A. Lemke

This study shows phosphorylation of TDP-43's low-complexity domain shifts its self-assembly from macrophase separation to micellization, potentially protecting against pathological aggregation.

Advanced Science · Jul 28, 2026Peer-reviewedBiophysics

Structural defects in amyloid-β fibrils drive secondary nucleation

Jing Hu, Tom Scheidt, Dev Thacker, Emil Axell, Elin Stemme, Urszula Łapińska, Stefan Wennmalm, Georg Meisl, Samo Curk, María Paz Andreasen, Michele Vendruscolo, Paolo Arosio, Anđela Šarić, Jeremy D. Schmit, Tuomas P. J. Knowles, , Alexander J. Dear

This study shows that structural defects in amyloid-β fibrils are key sites for secondary nucleation, suggesting new strategies for drug design to inhibit amyloid disorders.

Nature Communications · Feb 18, 2026Peer-reviewedBiophysics